ExplorEnz: EC 7.2.4.3

Your query returned 1 entry. Printable version

7.2.4.3

Accepted name:

(S)-methylmalonyl-CoA decarboxylase (sodium-transporting)

Reaction:

(S)-methylmalonyl-CoA + Na⁺_{[side 1]} + H⁺_{[side 2]} = propanoyl-CoA + CO₂ + Na⁺_{[side 2]}

Other name(s):

methylmalonyl-coenzyme A decarboxylase (ambiguous); (S)-2-methyl-3-oxopropanoyl-CoA carboxy-lyase (incorrect); (S)-methylmalonyl-CoA carboxy-lyase (ambiguous)

Systematic name:

(S)-methylmalonyl-CoA carboxy-lyase (propanoyl-CoA-forming, sodium-transporting)

Comments:

This bacterial enzyme couples the decarboxylation of (S)-methylmalonyl-CoA to propanoyl-CoA to the vectorial transport of Na⁺ across the cytoplasmic membrane, thereby creating a sodium ion motive force that is used for ATP synthesis. It is a membrane-associated biotin protein and is strictly dependent on sodium ions for activity.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 37289-44-4

References:

1.	Galivan, J.H. and Allen, S.H.G. Methylmalonyl coenzyme A decarboxylase. Its role in succinate decarboxylation by Micrococcus lactilyticus. J. Biol. Chem. 243 (1968) 1253–1261. [PMID: 5646172]
2.	Hilpert, W. and Dimroth, P. Conversion of the chemical energy of methylmalonyl-CoA decarboxylation into a Na⁺ gradient. Nature 296 (1982) 584–585. [PMID: 7070502]
3.	Hoffmann, A., Hilpert, W. and Dimroth, P. The carboxyltransferase activity of the sodium-ion-translocating methylmalonyl-CoA decarboxylase of Veillonella alcalescens. Eur. J. Biochem. 179 (1989) 645–650. [DOI] [PMID: 2920730]
4.	Huder, J.B. and Dimroth, P. Expression of the sodium ion pump methylmalonyl-coenzyme A-decarboxylase from Veillonella parvula and of mutated enzyme specimens in Escherichia coli. J. Bacteriol. 177 (1995) 3623–3630. [PMID: 7601825]
5.	Bott, M., Pfister, K., Burda, P., Kalbermatter, O., Woehlke, G. and Dimroth, P. Methylmalonyl-CoA decarboxylase from Propionigenium modestum^--cloning and sequencing of the structural genes and purification of the enzyme complex. Eur. J. Biochem. 250 (1997) 590–599. [PMID: 9428714]

[EC 7.2.4.3 created 1972 as EC 4.1.1.41, modified 1983, modified 1986, transferred 2018 to EC 7.2.4.3]